Personal-care articles having self-assembling peptides

ABSTRACT

A personal-care article, for receiving body exudates, having a self-assembling peptide is provided.

REFERENCE TO ELECTRONIC SUBMISSION OF A SEQUENCE LISTING

This application contains a Sequence Listing as an appendix on a compactdisc, as required under 37 C.F.R. §1.52(e)(1)(ii) and 37 C.F.R.§1.821(c), which is herein incorporated in its entirety in accordancewith 37 C.F.R. §1.77(b)(5). A duplicate disc for the sequence listing isalso provided. The compact disc and its duplicate are identical in theircontents. The compact disk contains a single ASCI (.txt) file for thesequence listing, the file is entitled “Self-assemblingpeptides_ST25.txt” and was created on 18 Jul. 2007 using a Windows XPProfessional, Version 2002, Service Pack 2 format, and is 8.0 mb insize. All files are Windows XP compatible. A statement that the file andits duplicate on the discs are identical is also submitted separately asrequired under 37 C.F.R. §1.52(e)(4).

FIELD OF THE INVENTION

The invention relates to personal-care articles, particularlypersonal-care articles having self-assembling peptides.

BACKGROUND OF THE INVENTION

Personal-care articles are well known for their ability to absorb bodilyexudates, for instance menses. Typically, personal-care articles, suchas feminine sanitary napkins, include a fluid-permeable topsheet thatfaces the body of a user, a fluid-impermeable backsheet, and anabsorbent core interposed between the topsheet and backsheet. Theabsorbent core is used to absorb and store the bodily exudates until thepersonal-care article has been removed.

Absorbent cores are designed not only to absorb an ever greater amountof bodily exudates, but also to store the bodily exudates more securely.The more bodily exudates absorbed by and stored in the personal-carearticle, the greater the chance that some of the absorbed bodilyexudates will exit from the personal-care article (rewet). Variouscauses can lead to rewet, such as material overload or physical stressesapplied to the personal-care article. Whatever the cause, leakage ofbodily exudates from a personal-care article is highly undesirable to auser.

The problem of increasing the amount of bodily exudate absorbed andstored by a personal-care article while reducing the occurrence of rewethas not been sufficiently solved by the current personal-care articles.Efforts to increase absorption and prevent rewet have focused onmodifying the absorbent core of a personal-care article. Suchmodifications have involved increasing the amount of absorbent materialin the absorbent core or adding materials, such as absorbent gellingmaterials to the absorbent core. The disadvantage of adding morematerial to the absorbent layer is that the additional materialincreases the absorbent core's size and thickness. This adds greaterweight to the personal-care article making it more difficult to wear.

It would be desirable to have a personal-care article that absorbs andstores greater amounts of bodily exudate than current personal-carearticles. Additionally, it would be desirable to have a personal-carearticle that could reduce the occurrence of rewet.

SUMMARY OF THE INVENTION

A personal-care article for receiving body exudates is provided thatcomprises at least one layer including a self-assembling peptide thatforms a matrix upon exposure to a bodily exudate.

A tampon is also provided that comprises an absorbent member, whereinthe tampon comprises a self-assembling peptide that forms a matrix uponexposure to a bodily exudate.

In addition, a method of storing a bodily exudate in a personal-carearticle is provided. The method comprises providing a personal-carearticle comprising a self-assembling peptide, and exposing thepersonal-care article to a bodily exudate. Upon exposure to the bodilyexudate the self-assembling peptide forms a matrix.

BRIEF DESCRIPTION OF THE DRAWINGS

FIG. 1 is a perspective view of a feminine sanitary napkin of thepresent invention.

FIG. 2 is a cross-sectional view of section A-A of FIG. 1.

FIG. 3 is a perspective view of a tampon of the present invention.

FIG. 4 is a cross-sectional view of section B-B of FIG. 3.

DETAILED DESCRIPTION OF THE INVENTION

The present invention provides a personal-care article, such as afeminine sanitary napkin, having self-assembling peptides. It isbelieved that the presence of self-assembling peptides in apersonal-care article can provide for increased storage capacity of thepersonal-care article and reduced rewet (the amount of stored bodilyexudate, such as menses, that exits the personal-care article duringwear). Upon contact with bodily exudates, the self-assembling peptidespresent in the personal-care article self-assemble into a matrix. Thematrix can serve to substantially immobilize the bodily exudates in thepersonal-care article, such that the bodily exudates cannot readily exitout of the personal-care article or move to other areas of thepersonal-care article. Therefore, the matrix formed from theself-assembling peptides provides the personal-care article with greatercontrol of absorbed bodily exudates.

As used herein, the term “personal-care article” refers to articles thatabsorb, block, or contain bodily exudates discharged from the body, andwhich may be placed within, against or in proximity to the body of auser. Examples of personal-care articles include feminine sanitarynapkins, tampons, and interlabial pads, adult incontinence products,training pants, and baby diapers.

As used herein, the term “bodily exudate” is any fluid produced anddischarged by a human body or animal body such as menses, urine, vaginalsecretions and the like.

As used herein, the term “menses” is a bodily exudate including blood,vaginal secretions and endometrial tissue. The vaginal secretions aremainly composed of mucins. Further, the blood present in menses differsfrom blood in circulation within the body, in that the blood present inmenses does not usually clot, as it is low in fibrinogen. Additionally,in contrast to blood within the body, the blood in menses is oftenenclosed within or attached to endometrial tissue.

The term “self-assembling peptide” as used herein refers to a peptideformed from a chain of at least two amino acids (α-amino acid residues)linked by covalent bonds, such as peptide bonds, wherein the peptidesself-assemble to form matrices upon contact with bodily exudates.Self-assembling peptides may also be branched, in which case they willcontain at least two amino acid chains linked by a non-peptide bond.Further, self-assembling peptides can vary in length so long as they canself-assemble. While the amino acid sequences of the self-assemblingpeptides can vary, in certain embodiments, sequences may include thosethat provide an amphiphilic nature to the self-assembling peptides, forexample the self-assembling peptides can include approximately equalnumbers of hydrophobic and hydrophilic amino acids.

The term “self-assemble” as used herein refers to the ability ofself-assembling peptides, without requiring the presence of a catalystor material processing, to form matrices upon exposure to bodilyexudates.

The term “matrix” as used herein is a gel structure that is formed whenself-assembling peptides are exposed to bodily-fluids. Upon exposure tobodily exudates self-assembling peptides form nanofibers that furtherform a matrix. While not being limited to theory, it is believed that asthe nanofibers form a matrix, bodily exudates are contained within thematrix and substantially immobilized, thus inhibiting further movementof the bodily exudates.

The self-assembling peptides may have, a chain of amino acids conformingto one or more of formulas (A)-(D):

TABLE 1 (A) ((Xaa^(neu) − Xaa⁺)_(x)(Xaa^(neu) − Xaa⁻)_(y))_(n) (B)((Xaa^(neu) − Xaa⁻)_(x)(Xaa^(neu) − Xaa⁺)_(y))_(n) (C) ((Xaa⁺ −Xaa^(neu))_(x)(Xaa⁻ − Xaa^(neu))_(y))_(n) (D) ((Xaa⁻ −Xaa^(neu))_(x)(Xaa⁺ − Xaa^(neu))_(y))_(n)

where: Xaa^(neu) represents an amino acid having a neutral charge atphysiological pH; Xaa⁺ represents an amino acid having a positive chargeat physiological pH; Xaa⁻ represents an amino acid having a negativecharge at physiological pH; x and y are integers having a value of 1-4,independently; and n has a value of 1-10.

The self-assembling peptides may have a chain of amino acids whereXaa^(neu) represents alanine, valine, leucine, isoleucine, or glycine;Xaa⁺ represents arginine, lysine or histidine; and Xaa⁻ representsaspartic acid or glutamic acid. For example, the self-assemblingpeptides may have, or may include, the amino acid sequence RADARADARADA(SEQ ID No: 28).

The matrices described herein can be formed through self-assembly of theself-assembling peptides described in U.S. Pat. Nos. 5,670,483;5,955,343; 6,548,630; and 6,800,481 and in Holmes et al., Proc. Natl.Acad. Sci. USA, 97:6728-6733 (2000); Zhang et al., Proc. Natl. Acad.Sci. USA, 90:3334-3338 (1993); Zhang et al., Biomaterials, 16:1385-1393(1995); Caplan et al., Biomaterials, 23:219-227 (2002); Leon et al., J.Biomaterials; Sci. Polym. Ed., 9:297-312 (1998); and Caplan et al.,Biomacromolecules, 1:627-631 (2000). Examples of self-assemblingpeptides are shown in Table 2.

TABLE 2 Name Sequence (n→c) Configuration RADA16-I n-RADARADARADARADA-c I (SEQ ID NO: 1) RGDA16-I n-RADARGDARADARGDA-c  I (SEQ ID NO: 2)RADA8-I n-RADARADA-c  I (SEQ ID NO: 3) RAD16-II n-RARADADARARADADA-c II(SEQ ID NO: 4) RAD8-II n-RARADADA-c II (SEQ ID NO: 5) EAKA16-In-AEAKAEAKABAKAEAK-c  I (SEQ ID NO: 6) EAKA8-I n-AEAKAEAK-c  I(SEQ ID NO: 7) RAEA16-I n-RAEARAEARAEARAEA-c  I (SEQ ID NO: 8) RAEA8-In-RAEARAEA-c  I (SEQ ID NO: 9) KADA16-I n-KADAKADAKADAKADA- c  I(SEQ ID NO: 10) KADA8-I n-KADAKADA-c  I (SEQ ID NO: 11) EAH16-IIn-AEAEAHAHAEAEAHAH-c II (SEQ ID NO: 12) EAH8-II n-AEAEAHAH-c II(SEQ ID NO: 13) EFK16-II n-FEFEFKFKFEFEFKFK-c II (SEQ ID NO: 14) EFK8-IIn-FEFKFEFK-c  I (SEQ ID NO: 15) ELK16-II n-LELELKLKLELELKLK-c II(SEQ ID NO: 16) ELK8-II n-LELELKLK-c II (SEQ ID NO: 17) EAK16-IIn-AEAEAKAKAEAEAKAK-c II (SEQ ID NO: 18) EAK12 n-AEAEAEAEAKAK-c IV/II(SEQ ID NO: 19) EAK8-II n-AEAEAKAK-c II (SEQ ID NO: 20) KAE16-IVn-KAKAKAKAEAEAEAEA-c IV (SEQ ID NO: 21) EAK16-IV n-AEAEAEAEAKAKAKAK-c IV(SEQ ID NO: 22) RAD16-IV n-RARARARADADADADA-c IV (SEQ ID NO: 23)DAR16-IV n-ADADADADARARARAR-c IV (SEQ ID NO: 24) DAR32-IVn-(ADADADADARARARAR)₂-c IV (SEQ ID NO: 25) EHK16 n-HEHEHKHKHEHEHKHK-cN/A (SEQ ID NO: 26) EHK8 n-HEHEHKHK-c N/A (SEQ ID NO: 27) RADA12-In-RADARADARADA-c  I (SEQ ID NO: 28) RAD12-II n-RARADADARARA-c II(SEQ ID NO: 29) “N/A” denotes not applicable.

The list presented in Table 2 is representative rather than exclusive.Other self-assembling peptides can be generated, that differ from thoselisted in Table 2, for example by replacing a single or multiple aminoacids, by inclusion or exclusion of a repeating quartet, or byincorporating one or more cysteine amino acids, as cysteine amino acidsmay bond with one another through the formation of disulfide bonds thatprovide increased mechanical strength to the matrices.

To provide for matrix formation, in certain embodiments, theself-assembling peptides are complementary and structurally compatible.For example, to be complementary, the side chains (amino acid R groups)of the self-assembling peptides, which have a β-sheet structure,partition into two faces, a first non-polar face with side chains thathave no charge (neutral) at physiological pH, for instance the sidechain of an alanine amino acid or other hydrophobic amino acid, and asecond polar face with positively or negatively charged ionic sidechains at physiological pH. The ionic side chains are complementary toone another in that positively charged and negatively charged aminoacids from individual self-assembling peptides can form complementaryionic pairs. For example, a negatively charged side chain from an aminoacid in a first self-assembling peptide can ionically bond with apositively charged side chain from an amino acid on a secondself-assembling peptide. These self-assembling peptides are thereforecalled complementary self-assembling peptides and, as shown in Table 2,have at least four different configurations, namely I, II, III, or IV.If the charged amino acids alternate with one positively and onenegatively charged amino acid on the polar face (−+−+−+−+), theself-assembling peptides are described as “configuration I;” if thecharged amino acids alternate with two positively and two negativelycharged residues (−−++−−++) on the polar face, the self-assemblingpeptides are described as “configuration II;” if the charged amino acidsalternate with three positively and three negatively charged residues(+++−−−+++−−−) on the polar face, the self-assembling peptides aredescribe as “configuration III;” if the charged amino acids alternatewith four positively and four negatively charged residues(++++−−−−++++−−−−) on the polar face, they are described as“configuration IV.” Configuration I-IV self-assembling peptides are alsorepresented in Table 1 by formulas (A)-(D). Formulas (A)-(D) representConfiguration I self-assembling peptides when x and y are both one,Configuration II self-assembling peptides when x and y are both two,Configuration III self-assembling peptides when x and y are both three,and Configuration IV self-assembling peptides when x and y are bothfour.

If the charged amino acids in self-assembling peptides are substitutedwith a like charge, there are no known significant effects on theself-assembly process. For example, positively charged lysines can bereplaced by positively charged arginines and negatively chargedglutamates can be replaced by negatively charged aspartates. However, ifthe positively charged residues (lysine and arginine) are replaced bynegatively charged residues (aspartate and glutamate), theself-assembling peptides can no longer undergo self-assembly to formmatrices, but they can still form a β-sheet structure in the presence ofa salt. Other amino acids that form hydrogen bonds, such as asparagineand glutamine, may be incorporated into the self-assembling peptidesinstead of, or in addition to, charged residues. By changing the alanineresidues in the self-assembling peptides to more hydrophobic residues,such as leucine, isoleucine, phenylalanine or tyrosine, the resultingself-assembling peptides have a greater tendency to self-assemble andform self-assembling peptide matrices with enhanced strength. Someself-assembling peptides that have similar amino acids compositions andlengths as the self-assembling peptides described herein form α-helicesand random-coils rather than β-sheets that do not form macroscopicmatrices. Thus, in addition to complementarity and structuralcompatibility other factors can, in certain embodiments, determine theformation of macroscopic matrices, such as the self-assembling peptidelength, the degree of intermolecular interaction, and the ability toform staggered arrays.

The self-assembling peptides are structurally compatible when they canmaintain a sufficiently constant intra self-assembling peptide distanceto allow matrix formation. While the intra self-assembling peptidedistance can vary, it can be quite small, for example less than about 4Å (angstroms). However, in certain embodiments the intra self-assemblingpeptide distance can be larger than this, such as about 10 Å. Thesedistances can be calculated based on molecular modeling such as thatdisclosed in U.S. Pat. No. 5,670,483, and in certain embodiments may bebased on an average of a representative number of distances.

The mixtures of self-assembling peptides as described herein, regardlessof the precise form, for example whether in a liquid or powdered form,may include RADA16-I (SEQ ID NO:1) or RADA12-I (SEQ ID NO:28) andEAKA16-I (SEQ ID NO:6) or EAK16-II (SEQ ID NO:18). Other mixtures caninclude RAD16-II (SEQ ID NO:4), EAKA16-I (SEQ ID NO:6), or EAK16-II (SEQID NO:18). In addition, other mixtures can include various lengths ofthe same self-assembling peptide sequence such as, RADA12-I and RADA16-Ior RAD12-II and RAD16-II, or mixtures of configuration I andconfiguration II self-assembling peptides such as RADA12-I and RAD12-IIor RADA16-I and RAD16-II. The use of mixtures of self-assemblingpeptides rather than a single self-assembling peptide can modulateproperties of matrices, such as the speed of assembly and the stiffnessof the matrix.

As described above, matrices can be formed of heterogeneous mixtures ofself-assembling peptides (mixtures containing more than one type ofself-assembling peptide conforming to a given formula, see table 1).However, in certain embodiments, the single type of self-assemblingpeptides present in a mixture is able to form a matrix byself-assembling. In other embodiments, a heterogeneous mixture of two ormore types of self-assembling peptides are used to form a matrix throughself-assembling. The self-assembling peptides can be chemicallysynthesized or purified from natural or recombinantly-produced sourcesby methods well known in the art. For example, self-assembling peptidescan be synthesized using standard fluorenylmethoxycarbonyl (Fmoc)chemistry and purified using high pressure liquid chromatography (HPLC).

The number of amino acids in self-assembling peptides can vary. Forexample, in certain embodiments, the self-assembling peptides maycontain between about 8 amino acids to about 200 amino acids, about 8 toabout 36 amino acids, or about 8 to about 16 amino acids. In addition toL-form amino acids the amino acids that form the self-assemblingpeptides may be amino acid analogs; amino acids of the D-form; and aminoacids which have been altered or derivatized by the addition of achemical group such as an acyl group, a phosphate group, a farnesylgroup, an isofarnesyl group, or a fatty acid group. Further, the aminoacids of the self-assembling peptides can be naturally occurring ornon-naturally occurring amino acids. Non-naturally occurring amino acidshave not been found in nature, but can be incorporated into aself-assembling peptide chain, for exampleD-alloisoleucine(2R,3S)-2-amino-3-methylpentanoic acid and L-cyclopentylglycine (S)-2-amino-2-cyclopentyl acetic acid. Non-natural amino acidsand amino acid derivatives listed in U.S. Pub. No. 2004/0204561 can beused. Naturally-occurring hydrophobic amino acids include Ala, Val, Ile,Met, Phe, Tyr, Trp, Ser, Thr and Gly. The charged amino acids can bebasic (positive) amino acids, such as Lys, Arg, H is, and Orn; acidic(negative) amino acids, such as Glu and Asp; or amino acids that formhydrogen bonds, such as Asn and Gln.

The carboxyl-terminal residue (c-terminus), amino-terminal residue(n-terminus), or both of a self-assembling peptide may be modified. Forexample, the carboxyl group of the c-terminus, the amino group of then-terminus, or both can be modified. The charge at the c-terminus,n-terminus or both can also be modified. For example, a group or radicalsuch as an acyl group (RCO—, where R is an organic group such as, anacetyl group (CH₃CO—)) can be present at the n-terminus of aself-assembling peptide to neutralize an “extra” positive charge thatmay otherwise be present, such as a charge not resulting from the sidechain of the n-terminus amino acid. Similarly, a group such as an aminegroup (NH₂) in the form of an amide (CO—NH₂) can be used to neutralizean “extra” negative charge that may otherwise be present at thec-terminus, such as a charge not resulting from the side chain of thec-terminus amino acid. The neutralization of charges on a terminus maypromote the formation of matrices through self-assembly.

In certain embodiments, prior to self-assembly, the self-assemblingpeptides may be in the form of a solution by being dissolved oremulsified in a liquid, such as deionized water, that is substantiallyfree of ions such as monovalent ions, or contains a sufficiently lowconcentration of ions to prevent significant self-assembly of theself-assembling peptides. For example, a liquid with a concentration ofions less than about 5 mM could be used to form a solution.Self-assembly may be initiated or enhanced at any subsequent time by theaddition of a bodily exudate, such as menses. A wide variety of ions,including anions and cations whether divalent, monovalent, or trivalent,can be used. For example, matrix formation may be promoted by exposureto monovalent cations such as Li⁺, Na⁺, K⁺, and Cs⁺, and theconcentration of such ions used to induce or enhance self-assembly istypically at least 5 mM. Lower concentrations also facilitate assembly,though at a reduced rate. For example, NaCl at a concentration ofbetween about 5 mM and about 5 M will induce the assembly of matriceswithin a few minutes. Concentrations of NaCl below 5 mM may also inducematrix assembly, but at a slower rate.

The concentration of self-assembling peptides in a solution or powderformulation can vary. For example, the concentration of self-assemblingpeptides in a solution can be from about 0.01% w/v (0.1 mg/ml) to about99% w/v (990 mg/ml), inclusive. In certain embodiments, theconcentration of self-assembling peptides prior to forming the matrixcan be between about 0.1% (1 mg/ml) and about 10% (100 mg/ml). In someembodiments, the concentration of self-assembling peptides may also beless than about 0.1%. The self-assembling peptides can also beformulated as powders and administered in a powder form. In certainembodiments, powder formulations may have a concentration ofself-assembling peptides of about 100%. The concentration ofself-assembling peptides can be higher in stock solutions and powderedformulations. The concentration can then be brought to the desired levelbefore use by addition of a diluent, such as deionized water or otherpowders that do not contain self-assembling peptide.

In certain embodiments, self-assembling peptides can be delivered with ahydrophobic material, such as a pharmaceutically acceptable oil, in aconcentration that permits self-assembly, but at a reduced rate. Whenself-assembling peptides are mixed with a hydrophobic agent such as anoil or lipid the assembly of the self-assembling peptides into a matrixdiffers from matrix formation in an aqueous environment. The hydrophilicpart of the peptide will assemble in such a way to minimize contact withthe hydrophobic material, thereby creating a barrier between the twoenvironments. This type of behavior enables the encapsulation oftherapeutics or other molecules that can be released from the matrixupon contact with bodily exudates.

Matrix formation through self-assembly may be initiated by components inbodily exudates such as ions, physiological pH of bodily exudates, orthe increase in temperature provided by contact with bodily exudates. Inone embodiment, the time for self-assembly of a matrix can be 60 secondsor less following contact with bodily exudates, such as menses. In somecircumstances, such as where the concentration of self-assemblingpeptides is low, self-assembly may take longer, for example, up to aminute, 5 minutes, 10 minutes, 30 minutes, an hour, or longer.

When the self-assembling peptides are exposed to bodily exudates theself-assembling peptides form nanofibers that further formthree-dimensional porous matrices. In certain embodiments, thenanofibers may be about 10 nm to about 20 nm in diameter, and form poresin a matrix, wherein the pores have a greatest width dimension of about50 nm to about 100 nm. The matrices can have dimensions large enough tobe visible under low magnification, such as about 10-fold or less.

The properties and mechanical strength of the matrices can be controlledthrough manipulation of the self-assembling peptides contained therein.For example, self-assembling peptides can form matrices having varyingdegrees of stiffness or elasticity. In certain embodiments, a matrix maybe somewhat deformable or compressible after self-assembly, butgenerally will not substantially flow from one area to another. Thematrices typically have a low elastic modulus, for example, in certainembodiments a matrix may have a modulus in the range of from about 1 kPato about 10 kPa as measured by methods known in the art, such as in astandard cone-plate rheometer. In certain embodiments, a matrix may havea lower elastic modulus (<1 kPa), as the lower value permits structuraldeformation of the matrix in response to pressure. Stiffness of thematrix can be controlled in a variety of ways, such as by any one ormore of the following including changing the length, sequence, orconcentration of the self-assembling peptides. Other methods forincreasing stiffness can also be employed, such as attaching to aself-assembling peptide, binding molecules that can be subsequentlycross-linked or otherwise bonded to one another, such as biotinmolecules or amino acids with aromatic rings. The binding molecules canbe included at the n- or c-terminus of a self-assembling peptide orattached to one or more amino acids between the termini. Thecross-linking of binding molecules may be done in any manner known inthe art. For example, biotin may be cross-linked using subsequentaddition of avidin, and amino acids having aromatic rings may becross-linked by exposure to UV light. The extent of cross-linking can bedetermined by light scattering, gel filtration, or scanning electronmicroscopy using methods known in the art. Furthermore, cross-linkingcan be examined by HPLC or mass spectrometry analysis of the matrixafter digestion with a protease, such as matrix metalloproteases.Material strength may be determined before and after cross-linking.

Further, the matrices formed can be characterized using variousbiophysical and optical techniques, such as circular dichroism (CD),dynamic light scattering, Fourier transform infrared (FTIR), atomicforce (tension) microscopy (ATM), scanning electron microscopy (SEM),and transmission electron microscopy (TEM). The matrices can also beexamined using several standard mechanical testing techniques to measurethe extent of swelling, the effect of pH and ion concentration on matrixformation, the level of hydration under various conditions, the tensilestrength, as well as the manner in which various characteristics changeover the period of time required for the matrices to form and degrade.These methods allow one of ordinary skill in the art to determine whichof the various alternatives and self-assembling peptides describedherein are most suitable for use in a specific application.

In certain embodiments, self-assembling peptides may be used to absorband store bodily exudates, such as menses in a personal-care article,for instance a feminine sanitary napkin. Personal-care articles are wellknown in the art and generally comprise nonwoven materials. Examples ofpersonal-care articles include feminine sanitary napkins, tampons,interlabial pads, adult incontinence products, training pants, and babydiapers. Any layer of a personal-care article may compriseself-assembling peptides. For example, if the personal-care article is afeminine sanitary napkin the self-assembling peptide could be present onor in the topsheet, backsheet, or absorbent core. Further, theself-assembling peptide may be present substantially throughout anylayer of a personal-care article, or only in certain areas of a layer.For instance, the self-assembling peptides could be applied only to thearea or surface of an absorbent core that will be positioned under thevaginal opening. Further still, the self-assembling peptides can beapplied to any surface of a layer, such as the body facing surface of abacksheet.

The self-assembling peptides may be applied to a personal-care articleas a dry or lyophilized powder or a liquid wherein the self-assemblingpeptide is suspended or dissolved in a liquid such as deionized water,or any other form of self-assembling peptide. When in liquid form, theself-assembling peptide may be applied to a personal-care article as aspray, paint, print, injection, or any other method known in the art. Incertain embodiments, whether in powder or liquid form, an amount of fromabout 0.1 grams per square meter (g/m²) to about 500 g/m² ofself-assembling peptide is present on or in the personal-care article.In other embodiments, an amount of from about 1 g/m² to about 100 g/m²self-assembling peptide is present on or in the personal-care article.In general, the amount of self-assembling peptide present on or in apersonal-care article will vary depending on various factors such as thesize of the area to which the self-assembling peptide is applied, or thetype of personal-care article. The device used to deliver the materialwill vary in accordance with the amount.

An example of a personal-care article for receiving body exudates, inthis instance a feminine sanitary napkin 30, having the self-assemblingpeptide included in a layer is shown in FIG. 1. A cross-section of asuitable feminine sanitary napkin 30 is shown in FIG. 2 that illustratesthe layers of the particular feminine sanitary napkin 30 shown, namelythe topsheet 34, backsheet 36, and absorbent core 38.

The topsheet 34 of the feminine sanitary napkin 30 is oriented towardsand contacts the body of a wearer to receive bodily discharges. Incertain embodiments, the topsheet 34 is liquid pervious, and may beflexible and nonirritating to the skin. Topsheets 34 may be made fromnonwoven materials or perforated polyolefinic films or other suitablematerials. In certain embodiments, the topsheet 34 may include aplurality of apertures to permit liquids deposited thereon to passthrough to the absorbent core 38. Exemplary suitable topsheets 34 may bemade in accordance with U.S. Pat. No. 4,342,314 and U.S. Pat. No.4,463,045.

The backsheet 36 may be any flexible material. In certain embodiments,it may be desirable that the backsheet or a portion thereof is liquidresistant or liquid impervious. The backsheet may, for example include apolyolefinic film, such as a polyethylene film. The backsheet 36prevents menses absorbed by and stored in the feminine sanitary napkin30, and particularly menses absorbed by the absorbent core 38, fromexiting the feminine sanitary napkin 30 and soiling the clothing andbedding of the wearer. In certain embodiments, the backsheet 36 may alsobe impervious to malodorous gases generated by absorbed bodilydischarges, so that the malodors do not escape and become noticed by thewearer. In certain other embodiments, the backsheet 36 may also permitgases or vapors to pass through it so that it is breathable, while stillresisting the passage of liquids there through. Further, the backsheet36 may be made of a soft cloth-like material for example, a polyester orpolyolefinic fiber backsheet 36. In certain embodiments, a softcloth-like backsheet 36 material may be a laminate of a polyesternon-woven material lamina, and a film such as described in U.S. Pat. No.4,476,180.

The absorbent core 38 of the feminine sanitary napkin 30 absorbs andstores menses, particularly menses that traverses through the liquidpermeable topsheet 34. In certain embodiments, the absorbent core 38 maystore between about four grams to about six grams of menses. Like thetopsheet 34 and backsheet 36, the absorbent core 38 may be conformableand nonirritating to the skin. In certain embodiments, the absorbentcore 38 may be rectangular or hourglass shaped. In certain embodiments,the absorbent core 38 has two opposed surfaces, one oriented towards thebacksheet 36, and one oriented towards the topsheet 34.

The absorbent core 38 may comprise absorbent material. The absorbentmaterial may comprise airfelt, such as cellulose wadding and fibratedcommunition pulp; tissue paper; absorbent gelling materials; foam; orcombinations thereof. Exemplary suitable tissue paper may include tissuepaper made in accordance with U.S. Pat. No. 4,191,609 may be used.Exemplary suitable absorbent gelling materials may include absorbentgelling materials made in accordance with U.S. Pat. Re. No. 32,649.Exemplary suitable foam may include foam made in accordance with U.S.Pat. No. 5,260,345 and U.S. Pat. No. 5,387,207.

In certain embodiments, the absorbent core 38 is interposed between thetopsheet 34 and backsheet 36. This prevents the absorbent material ofthe absorbent core 38 from shredding or becoming detached while thefeminine sanitary napkin 30 is worn, and to ensure proper containment ofmenses. The absorbent core 38 may be joined to the topsheet 34 andbacksheet 36. Joining may be by bonding the absorbent core 38 to thetopsheet 34, or the backsheet 36, using an adhesive. Such adhesive maybe applied in a spray pattern, such as a spiral or longitudinallyoriented beads.

The self-assembling peptide may be present in at least one of the layersof the feminine sanitary napkin 30, namely the topsheet 34, backsheet36, or absorbent core 38. For example, as shown in FIG. 2 theself-assembling peptide 42 may be present in the absorbent core 38 ofthe sanitary napkin 30, as the absorbent core 38 absorbs and storesmenses. It is believed, the presence of the self-assembling peptide 42in the absorbent core 38 of the feminine sanitary napkin 30 provides atleast two advantages over prior art feminine sanitary napkins. First,the self-assembling peptides increase the absorbent capacity of theabsorbent core by maintaining the absorbed menses in the areas of theabsorbent core that initially absorbed the menses. Therefore, the areasof the absorbent core that did not initially absorb the menses remaindry and retain the ability to absorb any additional menses. Second, byimmobilizing menses in the absorbent core, the self-assembling peptides,through matrix formation, prevent absorbed menses from exiting out ofthe absorbent core and contacting the body or undergarments of a user.

A further example of a personal-care article, in this instance a tampon50, having the self-assembling peptide is shown in FIG. 3. The tampon 50is designed to be inserted into a woman's vaginal cavity to preventmenses from exiting the vaginal opening by contacting and absorbing theflow of menses. The tampon 50 comprises an absorbent member 52, whichmay be generally cylindrical shaped and a withdrawal means 54. Thewithdrawal means 54 may be attached to the absorbent member 52, by anymanner known in the art, such as sewing, adhesive, thermal bonding,fusion bonding, or combinations thereof.

The absorbent member 52 of the tampon 50 may be constructed fromabsorbent materials such as fibrous materials. Such fibrous materialsmay include, but are not limited to synthetic fibers, natural fibers, orcombinations thereof. The natural fibers may include, but are notlimited to, cotton, wood pulp, flax, hemp, and rayon, such as GALAXYRayon (a tri-lobed rayon structure) available as 6140 Rayon; or SARILLEL rayon (a round fiber rayon), both available from Kelheim Fibers ofKelheim, Germany, cotton, wood pulp, flax, and hemp. The syntheticfibers can include, but are not limited to, fibers such as polyester,polyolefin, nylon, polypropylene, polyethylene, polyacrylic, vinylpolyacetate, polyacrylate, cellulose acetate, or bicomponent fibers,such as bicomponent polyethylene and polypropylene fibers. Additionalabsorbent material include materials such as, peat moss, absorbent foams(such as those disclosed in U.S. Pat. No. 3,994,298), capillary channelfibers (such as those disclosed in U.S. Pat. No. 5,356,405), highcapacity fibers (such as those disclosed in U.S. Pat. No. 4,044,766),superabsorbent polymers or absorbent gelling materials (such as thosedisclosed in U.S. Pat. No. 5,830,543), may be incorporated into thetampon.

In certain embodiments, as shown in FIG. 3, an absorbent member 52 maybe substantially covered by an overwrap 56, such as those described inU.S. Pat. No. 6,840,927. The overwrap 56 may be formed from nonwovenfibrous materials or apertured films.

The self-assembling peptide 42 may be present in any layer of the tampon50, such as the overwrap 56 or absorbent member 52. In certainembodiments, as shown in FIG. 4, which is a cross-sectional view of FIG.3, the self-assembling peptide 42 may be present in the absorbent member52 as the absorbent member 52 collects and absorbs menses. It isbelieved, the presence of the self-assembling peptide 42 in theabsorbent member 52 provides the tampon 50 with the advantages overprior art tampons such as increased absorptive capacity as notedpreviously with reference to the feminine sanitary napkin. In addition,it is further believed the self-assembling peptide reduces the amount ofmenses lost by a tampon in response to external pressure. As the tamponis in a confined space (the vaginal cavity) the tampon is oftensubjected to external pressure, especially during removal, which cancause menses to be forced or squeezed out of the tampon. However, as themenses may be immobilized in the matrix formed by the self-assemblingpeptides the amount of menses lost from the tampon during wear orremoval is reduced.

The dimensions and values disclosed herein are not to be understood asbeing strictly limited to the exact numerical values recited. Instead,unless otherwise specified, each such dimension is intended to mean boththe recited value and a functionally equivalent range surrounding thatvalue. For example, a dimension disclosed as “40 mm” is intended to mean“about 40 mm.”

All documents cited in the Detailed Description of the Invention are, inrelevant part, incorporated herein by reference; the citation of anydocument is not to be construed as an admission that it is prior artwith respect to the present invention. To the extent that any meaning ordefinition of a term in this document conflicts with any meaning ordefinition of the same term in a document incorporated by reference, themeaning or definition assigned to that term in this document shallgovern.

While particular embodiments of the present invention have beenillustrated and described, it would be obvious to those skilled in theart that various other changes and modifications can be made withoutdeparting from the spirit and scope of the invention. It is thereforeintended to cover in the appended claims all such changes andmodifications that are within the scope of this invention.

1. A feminine sanitary napkin for receiving body exudates comprising: atopsheet, absorbent core, and backsheet; wherein, the absorbent coreincludes a self-assembling peptide that forms a matrix upon exposure toa bodily exudate, wherein the amino acid sequence of the self-assemblingpeptide comprises at least one of SEQ ID NO: 1 or SEQ ID NO: 28, whereinthe self-assembling peptide is in the form of at least one of a powderor solution.
 2. The personal-care article of claim 1, wherein theself-assembling peptide is a powder.
 3. The personal-care article ofclaim 1, wherein the self-assembling peptide is in a solution.
 4. Thepersonal-care article of claim 1, wherein the self-assembling peptide ispresent in the personal-care article in an amount of from about 0.1 g/m²to about 500 g/m².
 5. The personal-care article of claim 1, wherein theself-assembling peptide is present in the personal-care article in anamount of from about 1 g/m² to about 100 g/m².
 6. The personal-carearticle of claim 1, wherein the bodily exudate is menses.
 7. Thepersonal-care article of claim 1, wherein the self-assembling peptide iscomplementary and structurally compatible.